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- W2053982209 abstract "Circular dichroism (CD) spectroscopy can provide valuable information on membrane protein structures, including determination of secondary structures of intact proteins and domains, detection of conformational changes associated with binding ligands and different functional states, examination of environmental effects and intermolecular interactions associated with complex formation, and monitoring protein folding and membrane insertion processes. This dynamic information can be a valuable complement to the more detailed structural information produced by crystallography and NMR spectroscopy. Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy, which uses the intense light of a synchrotron for the measurements, has a number of advantages for membrane protein studies over conventional CD spectroscopy: The higher penetration of the light means proteins can be examined in detergents and lipid environments, as well as in high salts and buffer conditions used for crystallisation, so comparisons can be made as to the physiological relevance of structures. In addition it permits the use of high lipid-to-protein ratios which are more similar to native membranes. The higher signal-to-noise levels in SRCD enable the use of smaller amounts of protein and the detection of smaller conformational changes, as well as the detection of faster dynamic processes over a wider wavelength range. The lower wavelength data measurable improve the accuracy of secondary structure determinations and provide additional information on supersecondary motifs and folds. Plus, using oriented SRCD it is possible to determine the dispositions of different structural elements with respect to the membrane. I will use voltage-gated sodium channels as a case study demonstrating the types of information that can be gleaned from CD and SRCD studies, including ligand and drug binding, thermal stability, and comparisons of wildtype, modified and mutant proteins. This work was supported by grants from the U.K. BBSRC." @default.
- W2053982209 created "2016-06-24" @default.
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- W2053982209 date "2010-01-01" @default.
- W2053982209 modified "2023-10-16" @default.
- W2053982209 title "Using Circular Dichroism (CD) and Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy to Study Membrane Proteins" @default.
- W2053982209 doi "https://doi.org/10.1016/j.bpj.2009.12.1124" @default.
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